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Protein

Peroxisomal trans-2-enoyl-CoA reductase

Gene

PECR

Organism
Cavia porcellus (Guinea pig)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Participates in chain elongation of fatty acids. Has no 2,4-dienoyl-CoA reductase activity.

Catalytic activityi

Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH.1 Publication

Kineticsi

  1. KM=11 µM for decenoyl-CoA1 Publication
  2. KM=53 µM for NADPH1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei178 – 1781Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi23 – 4725NADPBy similarityAdd
BLAST

GO - Molecular functioni

  1. trans-2-enoyl-CoA reductase (NADPH) activity Source: UniProtKB

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-UniPathway
  2. phytol metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

SABIO-RKQ9JIF5.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal trans-2-enoyl-CoA reductase (EC:1.3.1.38)
Gene namesi
Name:PECR
OrganismiCavia porcellus (Guinea pig)
Taxonomic identifieri10141 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia
ProteomesiUP000005447: Unplaced

Subcellular locationi

Peroxisome 1 Publication

GO - Cellular componenti

  1. intracellular membrane-bounded organelle Source: UniProtKB
  2. mitochondrion Source: UniProtKB
  3. peroxisomal membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 302301Peroxisomal trans-2-enoyl-CoA reductasePRO_0000054739Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycineBy similarity
Modified residuei32 – 321N6-succinyllysineBy similarity
Modified residuei49 – 491PhosphoserineBy similarity
Modified residuei83 – 831N6-acetyllysineBy similarity
Modified residuei178 – 1781PhosphotyrosineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Expressioni

Tissue specificityi

Expressed in liver.1 Publication

Interactioni

Subunit structurei

Interacts with PEX5, probably required to target it into peroxisomes.By similarity

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000010538.

Structurei

3D structure databases

ProteinModelPortaliQ9JIF5.
SMRiQ9JIF5. Positions 8-302.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi300 – 3023Microbody targeting signalBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00760000118868.
HOVERGENiHBG105268.
InParanoidiQ9JIF5.
OMAiMLADIWG.
OrthoDBiEOG7Q5HFK.
TreeFamiTF315256.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PRINTSiPR00081. GDHRDH.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9JIF5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSWTKCQSC LAPGLLQNRA AIVTGGGTGI GKAIAKELLH LGCNVVIASR
60 70 80 90 100
KFDRLRAAAE ELKATLPPSN KAEVTPIQCN IRKEEEVNNL MKSTLALYGK
110 120 130 140 150
IDFLVNNGGG QFWSSPEHIS SKGWHAVIET NLTGTFYMCK AAYNSWMKEH
160 170 180 190 200
GGAIVNIIIL LNGQPFVAHS GAARGGVYNL TKSLALGWAR SGIRINCVAP
210 220 230 240 250
GTVYSQTAMD NYGDMGKTLF ADAFQKIPAK RLGVPEEVSS LVCFLLSPAA
260 270 280 290 300
SFITGQLVNV DGGQSLYCQN HDIPDHDNWP EGVGDLSTVK KMKESFKQKA

KL
Length:302
Mass (Da):32,529
Last modified:October 1, 2000 - v1
Checksum:i9C1430D90D4C07C2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF232010 mRNA. Translation: AAF69799.1.
RefSeqiXP_003462124.1. XM_003462076.2.

Genome annotation databases

EnsembliENSCPOT00000011831; ENSCPOP00000010538; ENSCPOG00000011717.
GeneIDi100725791.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF232010 mRNA. Translation: AAF69799.1.
RefSeqiXP_003462124.1. XM_003462076.2.

3D structure databases

ProteinModelPortaliQ9JIF5.
SMRiQ9JIF5. Positions 8-302.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000010538.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSCPOT00000011831; ENSCPOP00000010538; ENSCPOG00000011717.
GeneIDi100725791.

Organism-specific databases

CTDi55825.

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00760000118868.
HOVERGENiHBG105268.
InParanoidiQ9JIF5.
OMAiMLADIWG.
OrthoDBiEOG7Q5HFK.
TreeFamiTF315256.

Enzyme and pathway databases

UniPathwayiUPA00094.
SABIO-RKQ9JIF5.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PRINTSiPR00081. GDHRDH.
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and expression of mammalian peroxisomal trans-2-enoyl-coenzyme A reductase cDNAs."
    Das A.K., Uhler M.D., Hajra A.K.
    J. Biol. Chem. 275:24333-24340(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 92-118, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Liver.

Entry informationi

Entry nameiPECR_CAVPO
AccessioniPrimary (citable) accession number: Q9JIF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: October 1, 2000
Last modified: March 4, 2015
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.